GAG_SRV1
ID GAG_SRV1 Reviewed; 658 AA.
AC P04022;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 115.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Core polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp24;
DE Contains:
DE RecName: Full=Phosphorylated protein pp18;
DE Contains:
DE RecName: Full=p12;
DE Contains:
DE RecName: Full=Capsid protein p27;
DE Contains:
DE RecName: Full=Nucleocapsid protein p14;
DE Contains:
DE RecName: Full=p4;
GN Name=gag;
OS Simian retrovirus SRV-1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11942;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3006247; DOI=10.1126/science.3006247;
RA Power M.D., Marx P.A., Bryant M.L., Gardner M.B., Barr P.J., Luciw P.A.;
RT "Nucleotide sequence of SRV-1, a type D simian acquired immune deficiency
RT syndrome retrovirus.";
RL Science 231:1567-1572(1986).
RN [2]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=24298557; DOI=10.1155/2013/984028;
RA Huang X., Cheng Q., Du Z.;
RT "A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
RT ribosomal frameshifting or readthrough in animal viruses.";
RL Biomed. Res. Int. 2013:984028-984028(2013).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: [Nucleocapsid protein p14]: Nucleocapsid protein.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag polyprotein;
CC IsoId=P04022-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P04024-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P04025-1; Sequence=External;
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC Phosphorylated protein pp24 and phosphorylated protein pp18 contains
CC two L domains: a PTAP/PSAP motif which interacts with the UEV domain of
CC TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin
CC ligase NEDD4. Both motifs contribute to viral release. The PSAP motif
CC acts as an additional L domain and promotes the efficient release of
CC the virions but requires an intact PPPY motif to perform its function.
CC {ECO:0000250|UniProtKB:P07567}.
CC -!- PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix
CC (MA) domain mediates the transport and binding of Gag polyproteins to
CC the host plasma membrane and is required for the assembly of viral
CC particles. {ECO:0000250|UniProtKB:P10258}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000250|UniProtKB:P07567}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000305|PubMed:24298557}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M11841; AAA47730.1; -; Genomic_RNA.
DR PDB; 2F76; NMR; -; X=2-99.
DR PDB; 2F77; NMR; -; X=2-99.
DR PDBsum; 2F76; -.
DR PDBsum; 2F77; -.
DR BMRB; P04022; -.
DR SMR; P04022; -.
DR EvolutionaryTrace; P04022; -.
DR Proteomes; UP000007228; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Cleavage on pair of basic residues;
KW Coiled coil; Host-virus interaction; Lipoprotein; Metal-binding; Myristate;
KW Phosphoprotein; Repeat; Ribosomal frameshifting; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT CHAIN 2..658
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000443126"
FT CHAIN 2..100
FT /note="Matrix protein p10"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040964"
FT CHAIN 101..217
FT /note="Phosphorylated protein pp24"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040966"
FT PROPEP 101..162
FT /evidence="ECO:0000305"
FT /id="PRO_0000040965"
FT CHAIN 163..217
FT /note="Phosphorylated protein pp18"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000443127"
FT CHAIN 218..300
FT /note="p12"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040967"
FT CHAIN 301..526
FT /note="Capsid protein p27"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040968"
FT CHAIN 527..622
FT /note="Nucleocapsid protein p14"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040969"
FT CHAIN 623..658
FT /note="p4"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040970"
FT ZN_FING 548..565
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 577..594
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 113..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 217..258
FT /evidence="ECO:0000255"
FT MOTIF 203..206
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT MOTIF 211..214
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT COMPBIAS 113..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 100..101
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 163..164
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 217..218
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 300..301
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 526..527
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 622..623
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P10258"
SQ SEQUENCE 658 AA; 73195 MW; 60929C787AF6923A CRC64;
MGQELSQHER YVEQLKQALK TRGVKVKYAD LLKFFDFVKD TCPWFPQEGT IDIKRWRRVG
DCFQDYYNTF GPEKVPVTAF SYWNLIKELI DKKEVNPQVM AAVAQTEEIL KTSSHTELTT
KPSQNPDLDL ISLDSDDEGA KGSSLKDKNL SCTKKPKRFP VLLTAQTSAD PEDPNPSEVD
WDGLEDEAAK YHNPDWPPFL TRPPPYNKAT PSAPTVMAVV NPKEELKEKI AQLEEQIKLE
ELHQALISKL QKLKTGNETV TSPETAGGFS RTPHWPGQHI PKGKCCASRE KEEQTPKDIF
PVTETVDGQG QAWRHHNGFD FTVIKELKTA ASQYGATAPY TLAIVESVAD NWLTPTDWNT
LVRAVLSGGD HLLWKSEFFE NCRETAKRNQ QAGNGWDFDM LTGSGNYSST DAQMQYDPGL
FAQIQAAATK AWRKLPVKGD PGASLTGVKQ GPDEPFADFV HRLITTAGRI FGSAEAGVDY
VKQLAYENAN PACQAAIRPY RKKTDLTGYI RLCSDIGPSY QQGLAMAAAF SGQTVKDFLN
NKNKEKGGCC FKCGRKGHFA KNCHEHIHNN SETKAPGLCP RCKRGKHWAN ECKSKTDSQG
NPLPPHQGNG LRGQPQAPKQ AYGAVSFVPA NKNNPFQSLP EPPQEVQDWT SVPPPTQY
